Proteomics

Dataset Information

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The human phosphoproteome map based on PRIDE data


ABSTRACT: This project contains raw data, intermediate files and results used to create the PRIDE human phosphoproteome map. The map is based on joint reanalysis of 110 publicly available human datasets. All relevant datasets were retrieved from the PRIDE database, and after manual curation, only assays that employed dedicated phospho-enrichment sample preparation strategies (e. g. metal oxide affinity chromatography, anti-P-Tyr antibodies, etc.) were included. Raw files were jointly processed with MaxQuant computational platform using standard settings (see Data Processing Protocol). In total, the joint analysis allowed identification of 252,189 phosphosites at 1% peptide spectrum match false discovery rate (PSM FDR) (MQ search results available in ‘txt-100PTM’ folder), of which 121,896 passed the additional 1% site localization FDR threshold (MQ search results available in ‘txt-001PTM’ folder).

INSTRUMENT(S): LTQ FT, LTQ Orbitrap, LTQ Orbitrap Velos, LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Platelet, Brain, Primary Cell, Liver, Lung, Cell Culture, Colon, Blood, Hela Cell

SUBMITTER: Andrew Jarnuczak  

LAB HEAD: Juan Antonio Vizcaino

PROVIDER: PXD012174 | Pride | 2019-02-13

REPOSITORIES: Pride

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Publications


Protein phosphorylation is a key post-translational modification regulating protein function in almost all cellular processes. Although tens of thousands of phosphorylation sites have been identified in human cells, approaches to determine the functional importance of each phosphosite are lacking. Here, we manually curated 112 datasets of phospho-enriched proteins, generated from 104 different human cell types or tissues. We re-analyzed the 6,801 proteomics experiments that passed our quality co  ...[more]

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